Evidence map›Paper›PMID 32877270›Full record

ArticleMolecular biology of the cell2020

PICH regulates the abundance and localization of SUMOylated proteins on mitotic chromosomes.

Victoria A Hassebroek, Hyewon Park, Nootan Pandey, Brooklyn T Lerbakken, Vasilisa Aksenova, Alexei Arnaoutov, Mary Dasso, Yoshiaki Azuma

Open access · bronzeAbstract read
In one paragraph

Article in Molecular biology of the cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.9field-weighted citation impact, top 27% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

10 citing papers in PubMed, 15 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Victoria A HassebroekDepartment of Molecular Biosciences, University of Kansas, Lawrence, KS 66045.
Hyewon ParkDepartment of Molecular Biosciences, University of Kansas, Lawrence, KS 66045.
Nootan PandeyDepartment of Molecular Biosciences, University of Kansas, Lawrence, KS 66045.
Brooklyn T LerbakkenDepartment of Molecular Biosciences, University of Kansas, Lawrence, KS 66045.
Vasilisa AksenovaDivision of Molecular and Cellular Biology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.
Alexei ArnaoutovDivision of Molecular and Cellular Biology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.
Mary DassoDivision of Molecular and Cellular Biology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.
Yoshiaki AzumaDepartment of Molecular Biosciences, University of Kansas, Lawrence, KS 66045.
University of Kansas · USNational Institutes of Health · US

Funding

SUMO family Ubiquitin-like Modifiers In Higher EukaryotesZIAHD001902 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI DASSO, MARY C. · 2009 to 2021
$6.3M
Regulation of Microtubule Function by Tubulin Carboxy-terminal TailsR01GM112893 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI MOORE, JEFFREY KYLE · 2015 to 2019
$1.5M
Regulation of kinetochore function by Topoisomerase IIR01GM112793 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI AZUMA, YOSHIAKI, CLARKE, DUNCAN J. · 2015 to 2018
$1.2M
Intramural NIH HHS ZIA HD001902NIGMS NIH HHS R01 GM112793NIGMS NIH HHS R01 GM112893
6 · The paper itself

Abstract

Proper chromosome segregation is essential for faithful cell division and if not maintained results in defective cell function caused by the abnormal distribution of genetic information. Polo-like kinase 1-interacting checkpoint helicase (PICH) is a DNA translocase essential for chromosome bridge resolution during mitosis. Its function in resolving chromosome bridges requires both DNA translocase activity and ability to bind chromosomal proteins modified by the small ubiquitin-like modifier (SUMO). However, it is unclear how these activities cooperate to resolve chromosome bridges. Here, we show that PICH specifically disperses SUMO2/3 foci on mitotic chromosomes. This PICH function is apparent toward SUMOylated topoisomerase IIα (TopoIIα) after inhibition of TopoIIα by ICRF-193. Conditional depletion of PICH using the auxin-inducible degron (AID) system resulted in the retention of SUMO2/3-modified chromosomal proteins, including TopoIIα, indicating that PICH functions to reduce the association of these proteins with chromosomes. Replacement of PICH with its translocase-deficient mutants led to increased SUMO2/3 foci on chromosomes, suggesting that the reduction of SUMO2/3 foci requires the remodeling activity of PICH. In vitro assays showed that PICH specifically attenuates SUMOylated TopoIIα activity using its SUMO-binding ability. Taking the results together, we propose a novel function of PICH in remodeling SUMOylated proteins to ensure faithful chromosome segregation.

Indexed as

CentromereChromosomesChromosome SegregationDNA-Binding ProteinsDNA HelicasesDNA Topoisomerases, Type IIHumansMitosisSumoylationDNA-Binding ProteinsDNA HelicasesDNA Topoisomerases, Type IIERCC6L protein, human

Identifiers

PMID32877270
PMCPMC7851874
OpenAlexW3082707417

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.